Moasser MM. Targeting the function of the HER2 oncogene in human cancer therapeutics. Oncogene 2007; 26(46): 6577-92.
Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW Jr, et al. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 2003; 421(6924): 756-60.
Wolf-Yadlin A, Kumar N, Zhang Y, Hautaniemi S, Zaman M, Kim HD, et al. Effects of HER2 overexpression on cell signaling networks governing proliferation and migration. Mol Syst Biol 2006; 2: 54.
Baker M. Upping the ante on antibodies. Nat Biotechnol 2005; 23(9): 1065-72.
Lesterhuis WJ, Haanen JB, Punt CJ. Cancer immunotherapy--revisited. Nat Rev Drug Discov 2011; 10(8): 591-600.
Kolkman JA, Law DA. Nanobodies – from llamas to therapeutic proteins. Drug Discovery Today Technol 2010; 7(2): 139-46.
Rahbarizadeh F, Rahimi jamnani F, Iri-Sofla FJ. Nanobody, New Agent for Combating Against Breast Cancer Cells. In: Gunduz E, Gunduz M. Breast Cancer - Current and Alternative Therapeutic Modalities. Rijeka: InTech; 2011. p. 347-70.
Rahimi Jamnani F, Rahbarizadeh F, Shokrgozar MA. Nanobodies: Promising Nanodevices for Immunotherapy. Nanotechnology 2011; 160 (11): 36-41. [Article in Farsi]
Behdani M, Zeinali S, Khanahmad H, Karimipour M, Asadzadeh N, Azadmanesh K, et al. Generation and characterization of a functional Nanobody against the vascular endothelial growth factor receptor-2; angiogenesis cell receptor. Mol Immunol 2012; 50(1-2): 35-41.
Ahmadvand D, Rasaee MJ, Rahbarizadeh F, Kontermann RE, Sheikholislami F. Cell selection and characterization of a novel human endothelial cell-specific nanobody. Mol Immunol 2009; 46(8-9): 1814-23.
Tse C, Gauchez AS, Jacot W, Lamy PJ. HER2 shedding and serum HER2 extracellular domain: biology and clinical utility in breast cancer. Cancer Treat Rev 2012; 38(2): 133-42.
Molina MA, Codony-Servat J, Albanell J, Rojo F, Arribas J, Baselga J. Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells. Cancer Res 2001; 61(12): 4744-9.
Wang J, Willumsen N, Zheng Q, Xue Y, Karsdal MA, Bay-Jensen AC. Bringing cancer serological diagnosis to a new level: focusing on HER2, protein ectodomain shedding and neoepitope technology. Future Oncol 2013; 9(1): 35-44.
Rahbarizadeh F, Rasaee MJ, Forouzandeh M, Allameh A, Sarrami R, Nasiry H, et al. The production and characterization of novel heavy-chain antibodies against the tandem repeat region of MUC1 mucin. Immunol Invest 2005; 34(4): 431-52.
Ahmadvand D, Rasaee MJ, Rahbarizadeh F, Mohammadi M. Production and characterization of a high-affinity nanobody against human endoglin.
Jamnani FR, Rahbarizadeh F, Shokrgozar MA, Ahmadvand D, Mahboudi F, Sharifzadeh Z. Targeting high affinity and epitope-distinct oligoclonal nanobodies to HER2 over-expressing tumor cells. Exp Cell Res 2012; 318(10): 1112-24.
Jamnani FR, Rahbarizadeh F, Shokrgozar MA, Mahboudi F, Ahmadvand D, Sharifzadeh Z, et al. T cells expressing VHH-directed oligoclonal chimeric HER2 antigen receptors: Towards tumor-directed oligoclonal T cell therapy. Biochim Biophys Acta 2014; 1840(1): 378-86.
Rahbarizadeh F, Rasaee MJ, Forouzandeh Moghadam M, Allameh AA, Sadroddiny E. Production of novel recombinant single-domain antibodies against tandem repeat region of MUC1 mucin. Hybrid Hybridomics 2004; 23(3): 151-9.
Haurum JS. Recombinant polyclonal antibodies: the
next generation of antibody therapeutics? Drug Discov Today 2006; 11(13-14): 655-60.
Ben-Kasus T, Schechter B, Lavi S, Yarden Y, Sela M. Persistent elimination of ErbB-2/HER2-overexpressing tumors using combinations of monoclonal antibodies: relevance of receptor endocytosis. Proc Natl Acad Sci U S A 2009; 106(9): 3294-9.
Vaneycken I, Devoogdt N, Van Gassen N, Vincke C, Xavier C, Wernery U, et al. Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer. FASEB J 2011; 25(7): 2433-46.
Sheikholeslami F, Rasaee MJ, Shokrgozar MA, Dizaji MM, Rahbarizadeh F, Ahmadvande D. Isolation of a Novel Nanobody Against HER-2/neu Using Phage Displays Technology. Lab Medicine 2010; 41(2): 69-76.
Zagozdzon R, Gallagher WM, Crown J. Truncated HER2: implications for HER2-targeted therapeutics. Drug Discov Today 2011; 16(17-18): 810-6.
Original Article
Sci J Iran Blood Transfus Organ 2014;11(2): 126-136
Enrichment of phage display library against breast cancer cells for isolation ofanti-HER2 camelid single domain antibodies
1Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran 2Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran 3National Cell Bank of Iran, Pasteur Institute of Iran, Tehran, Iran 4School of Allied Medical Sciences, Tehran University of Medical Sciences, Tehran, Iran
Abstract Background and Objectives
Breast cancer cells can be hidden from immune cells by shedding tumor markers such as HER2. The increased soluble HER2 (sHER2) concentrations are associated with the outcome of HER2-positive breast cancer and sensitivity to trastuzumab treatment. To this end, camelid single domain antibodies (VHH) with unique properties and binding ability are very striking targeting agents to detect sHER2.
Materials and Methods
By panning on HER2 negative and positive cells, an immune camel library was enriched against HER2 antigen. Affinity and specificity of four selected VHHs to HER2, detection of sHER2 and binding of selected VHHs to HER2 on breast cancer cells were investigated by ELISA.
Results
After cell panning and ELISA, four VHHs that recognized HER2 antigen better than negative control were identified. High affinity HER2 specific VHHs (1012-1013 M-1) were able to detect sHER2 (2 µg/ml). When the mixture of VHH and sMUC1 was added to HER2 coated-well, the VHH bound to HER2. RR4 and RR6 VHHs showed the highest binding to SKBR3 (HER2 expressing cell) (2±0.33 and 2.5±0.15, respectively) compared to HER2 negative cell (0.38 ± 0.17 and 0.4±0.12, respectively).
Conclusions
The HER2 status of a primary tumor and responses to treatment can be evaluated by measuring sHER2 as a biomarker by HER2 specific VHHs.
Key words: Genes٬ HER-2, Breast Cancer
Received: 20 May 2013 Accepted: 9 Dec 2013
Correspondence: Rahberizadeh F., PhD of Medical Biochemistry. Associate Professor of Medical Biotecnology. Department of Medical Biotechnology, Faculty of Medical Sciences, Tarbiat Modares University.
P.O. Box: 14115-331, Tehran, Iran. Tel: (+9821) 82883884 ; Fax: (+9821) 88013030
E-mail: Rahbarif@modares.ac.ir
Rahimi Jamnani F, Rahbarizadeh F, Shokrgozar M, Ahmadvand D, Mahboudi F. Enrichment of phage display library against breast cancer cells for isolation of anti-HER2 camelid single domain antibodies . Sci J Iran Blood Transfus Organ 2014; 11 (2) :126-136 URL: http://bloodjournal.ir/article-1-755-en.html